The aggregation of proteins or their digested fragments through β-sheet structures has a
great significance because it leads to neurodegenerative diseases, which are a problem of the aging
societies of the developed countries. Short peptides are typically used as models to study the formation
of specific structures. However, while the formation of α-helical structure was investigated thoroughly,
until recently, there have been much fewer studies on the formation of β-structure. In this review,
recent experimental and theoretical studies of β-hairpin-forming peptides, both model alaninebased
systems, and those based on the fragments of real proteins, are summarized with regard to the
role of hydrophobic, local, and Coulombic interactions. It is demonstrated that the presence of
charged residues can induce a bent structure not only owing to the formation of salt bridges if oppositely-
charged residues present at the ends of a sequence but also through shielding the hydrophobic
interior by like-charged residues at the end of the sequence.
Keywords: Protein folding, β-hairpin formation, acid-base equilibria, conformational ensembles, molecular dynamics.
Rights & PermissionsPrintExport